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- EMDB-3954: Cryo-EM structure of the human INO80 complex bound to nucleosome -
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Open data
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Basic information
Entry | Database: EMDB / ID: EMD-3954 | ||||||||||||
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Title | Cryo-EM structure of the human INO80 complex bound to nucleosome | ||||||||||||
![]() | map of human INO80 bound to nucleosome | ||||||||||||
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Function / homology | ![]() : / : / chromatin remodeling => GO:0006338 / ATP-dependent chromatin remodeler activity => GO:0140658 / promoter-enhancer loop anchoring activity / positive regulation of nuclear cell cycle DNA replication / regulation of DNA strand elongation / positive regulation of telomere maintenance in response to DNA damage / establishment of protein localization to chromatin / R2TP complex ...: / : / chromatin remodeling => GO:0006338 / ATP-dependent chromatin remodeler activity => GO:0140658 / promoter-enhancer loop anchoring activity / positive regulation of nuclear cell cycle DNA replication / regulation of DNA strand elongation / positive regulation of telomere maintenance in response to DNA damage / establishment of protein localization to chromatin / R2TP complex / dynein axonemal particle / Swr1 complex / RPAP3/R2TP/prefoldin-like complex / regulation of double-strand break repair / positive regulation of telomerase RNA localization to Cajal body / Ino80 complex / UV-damage excision repair / protein folding chaperone complex / box C/D snoRNP assembly / DNA duplex unwinding / regulation of chromosome organization / NuA4 histone acetyltransferase complex / protein deubiquitination / regulation of DNA replication / regulation of G1/S transition of mitotic cell cycle / mitotic sister chromatid segregation / TFIID-class transcription factor complex binding / regulation of embryonic development / MLL1 complex / Telomere Extension By Telomerase / positive regulation of double-strand break repair via homologous recombination / alpha-tubulin binding / negative regulation of tumor necrosis factor-mediated signaling pathway / negative regulation of megakaryocyte differentiation / RNA polymerase II core promoter sequence-specific DNA binding / spindle assembly / ATP-dependent activity, acting on DNA / protein localization to CENP-A containing chromatin / Chromatin modifying enzymes / regulation of DNA repair / Replacement of protamines by nucleosomes in the male pronucleus / CENP-A containing nucleosome / heterochromatin organization / epigenetic regulation of gene expression / Packaging Of Telomere Ends / Recognition and association of DNA glycosylase with site containing an affected purine / Cleavage of the damaged purine / Deposition of new CENPA-containing nucleosomes at the centromere / DNA helicase activity / nucleosomal DNA binding / Recognition and association of DNA glycosylase with site containing an affected pyrimidine / Cleavage of the damaged pyrimidine / Inhibition of DNA recombination at telomere / Meiotic synapsis / positive regulation of DNA repair / telomere organization / TBP-class protein binding / RNA Polymerase I Promoter Opening / Interleukin-7 signaling / telomere maintenance / Assembly of the ORC complex at the origin of replication / SUMOylation of chromatin organization proteins / DNA methylation / Condensation of Prophase Chromosomes / ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression / SIRT1 negatively regulates rRNA expression / Chromatin modifications during the maternal to zygotic transition (MZT) / HCMV Late Events / PRC2 methylates histones and DNA / innate immune response in mucosa / Defective pyroptosis / cellular response to estradiol stimulus / HDACs deacetylate histones / cellular response to ionizing radiation / RNA Polymerase I Promoter Escape / lipopolysaccharide binding / Nonhomologous End-Joining (NHEJ) / Transcriptional regulation by small RNAs / Formation of the beta-catenin:TCF transactivating complex / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / DNA Damage Recognition in GG-NER / double-strand break repair via homologous recombination / euchromatin / RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function / NoRC negatively regulates rRNA expression / Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3 / negative regulation of canonical Wnt signaling pathway / B-WICH complex positively regulates rRNA expression / G2/M DNA damage checkpoint / HDMs demethylate histones / DNA Damage/Telomere Stress Induced Senescence / Metalloprotease DUBs / chromatin DNA binding / PKMTs methylate histone lysines / ADP binding / Meiotic recombination / beta-catenin binding / RMTs methylate histone arginines / Pre-NOTCH Transcription and Translation / nuclear matrix Similarity search - Function | ||||||||||||
Biological species | ![]() | ||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 4.8 Å | ||||||||||||
![]() | Ayala R / Willhoft O / Aramayo RJ / Wilkinson M / McCormack EA / Ocloo L / Wigley DB / Zhang X | ||||||||||||
Funding support | ![]()
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![]() | ![]() Title: Structure and regulation of the human INO80-nucleosome complex. Authors: Rafael Ayala / Oliver Willhoft / Ricardo J Aramayo / Martin Wilkinson / Elizabeth A McCormack / Lorraine Ocloo / Dale B Wigley / Xiaodong Zhang / ![]() Abstract: Access to DNA within nucleosomes is required for a variety of processes in cells including transcription, replication and repair. Consequently, cells encode multiple systems that remodel nucleosomes. ...Access to DNA within nucleosomes is required for a variety of processes in cells including transcription, replication and repair. Consequently, cells encode multiple systems that remodel nucleosomes. These complexes can be simple, involving one or a few protein subunits, or more complicated multi-subunit machines . Biochemical studies have placed the motor domains of several chromatin remodellers in the superhelical location 2 region of the nucleosome. Structural studies of yeast Chd1 and Snf2-a subunit in the complex with the capacity to remodel the structure of chromatin (RSC)-in complex with nucleosomes have provided insights into the basic mechanism of nucleosome sliding performed by these complexes. However, how larger, multi-subunit remodelling complexes such as INO80 interact with nucleosomes and how remodellers carry out functions such as nucleosome sliding , histone exchange and nucleosome spacing remain poorly understood. Although some remodellers work as monomers , others work as highly cooperative dimers. Here we present the structure of the human INO80 chromatin remodeller with a bound nucleosome, which reveals that INO80 interacts with nucleosomes in a previously undescribed manner: the motor domains are located on the DNA at the entry point to the nucleosome, rather than at superhelical location 2. The ARP5-IES6 module of INO80 makes additional contacts on the opposite side of the nucleosome. This arrangement enables the histone H3 tails of the nucleosome to have a role in the regulation of the activities of the INO80 motor domain-unlike in other characterized remodellers, for which H4 tails have been shown to regulate the motor domains. | ||||||||||||
History |
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Structure visualization
Movie |
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Structure viewer | EM map: ![]() ![]() ![]() |
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 10.5 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 31 KB 31 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 9.7 KB | Display | ![]() |
Images | ![]() | 65.5 KB | ||
Others | ![]() | 63.1 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 258.2 KB | Display | ![]() |
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Full document | ![]() | 257.3 KB | Display | |
Data in XML | ![]() | 11.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6htsMC M: atomic model generated by this map C: citing same article ( |
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Similar structure data |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
File | ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Annotation | map of human INO80 bound to nucleosome | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.09 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 0 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
-Additional map: blurred map (with a factor applied of 250)...
File | emd_3954_additional.map | ||||||||||||
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Annotation | blurred map (with a factor applied of 250) to help visualise the nucleosome and flexible regions of the complex that have not been modelled | ||||||||||||
Projections & Slices |
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Density Histograms |
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Sample components
+Entire : Complex of core human INO80 with nucleosome
+Supramolecule #1: Complex of core human INO80 with nucleosome
+Supramolecule #2: nucleosome
+Supramolecule #4: human INO80
+Supramolecule #3: Histone subunits
+Macromolecule #1: RuvB-like 1
+Macromolecule #2: RuvB-like 2
+Macromolecule #3: DNA helicase INO80
+Macromolecule #4: Actin-related protein 5
+Macromolecule #5: Histone H3.1
+Macromolecule #6: Histone H4
+Macromolecule #7: Histone H2A type 1-B/E
+Macromolecule #8: Histone H2B type 1-J
+Macromolecule #9: INO80 complex subunit B
+Macromolecule #10: DNA (142-MER)
+Macromolecule #11: DNA (142-MER)
+Macromolecule #12: ADENOSINE-5'-DIPHOSPHATE
+Macromolecule #13: ZINC ION
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 8 |
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Vitrification | Cryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: FEI FALCON III (4k x 4k) / Detector mode: INTEGRATING / Average electron dose: 80.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |